ReviewToxins2017
Direct Fibrinolytic Snake Venom Metalloproteinases Affecting Hemostasis: Structural, Biochemical Features and Therapeutic Potential.
Review in Toxins, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
30 citing papers in PubMed, 72 citations in OpenAlex.
- Targeting Key Enzymatic Snake Venom Proteins Using Repurposed Small Molecule Inhibitors: Emerging Adjuncts to Antivenom Therapy.International journal of molecular sciences · 2026Review
- Review
- Snake Venom Protease Detection and Inhibition in Serum.ChemMedChem · 2026Article
- ProVenTL: a transfer-learning framework for predicting peptide-protein interactions derived from snake venom for cancer therapeutics.Journal of computer-aided molecular design · 2026Article
- Comprehensive molecular characterization and comparison of venom proteins and transcripts in three Gloydius species from South Korea.Scientific reports · 2026Article
- Neutrophil Inflammasome Activation and Pyroptosis Induced by a Metalloproteinase via HIF-1α and Gasdermin D Pathways.Journal of innate immunity · 2026Article
- Predictors and nomogram for amputation risk in pit viper snakebite envenoming at hospital admission.Scientific reports · 2025Article
- Bite First, Bleed Later: How PhilippineToxins · 2025Article
- Metabolomics and proteomics: synergistic tools for understanding snake venom inhibition.Archives of toxicology · 2025Review
- Article
- Article
- The Venom ofVeterinary sciences · 2024Article
- Article
- Review
- Bothrops venom-induced hemostasis disorders in the rat: Between Scylla and Charybdis.PLoS neglected tropical diseases · 2023Article
- Insight into the Toxicological and Pathophysiological Effects of Moroccan Vipers' Venom: Assessing the Efficacy of Commercial Antivenom for Neutralization.Tropical medicine and infectious disease · 2023Article
- Pictolysin-III, a Hemorrhagic Type-III Metalloproteinase Isolated fromPharmaceutics · 2023Article
- Cryo-EM structures show the mechanistic basis of pan-peptidase inhibition by human αProceedings of the National Academy of Sciences of the United States of America · 2022Article
- The rise of genomics in snake venom research: recent advances and future perspectives.GigaScience · 2022Article
- A comparative cross-reactivity and paraspecific neutralization study on Hypnale hypnale, Echis carinatus, and Daboia russelii monovalent and therapeutic polyvalent anti-venoms.PLoS neglected tropical diseases · 2022Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Snake venom metalloproteinases (SVMPs) are predominant in viperid venoms, which provoke hemorrhage and affect hemostasis and thrombosis. P-I class enzymes consist only of a single metalloproteinase domain. Despite sharing high sequence homology, only some of them induce hemorrhage. They have direct fibrin(ogen)olytic activity. Their main biological substrate is fibrin(ogen), whose Aα-chain is degraded rapidly and independently of activation of plasminogen. It is important to understand their biochemical and physiological mechanisms, as well as their applications, to study the etiology of some human diseases and to identify sites of potential intervention. As compared to all current antiplatelet therapies to treat cardiovascular events, the SVMPs have outstanding biochemical attributes: (a) they are insensitive to plasma serine proteinase inhibitors; (b) they have the potential to avoid bleeding risk; (c) mechanistically, they are inactivated/cleared by α2-macroglobulin that limits their range of action in circulation; and (d) few of them also impair platelet aggregation that represent an important target for therapeutic intervention. This review will briefly highlight the structure-function relationships of these few direct-acting fibrinolytic agents, including, barnettlysin-I, isolated from
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.